| Primary information |
|---|
| Hemolytik ID | 1091 |
| PMID | 17212422 |
| YEAR | 2007 |
| SEQUENCE | APC-L-ACPC-K-ACPC-L-APC-L-ACPC-K-ACPC-L-APC-L-ACPC |
| LENGTH | 15 |
| NAME | Peptide 1 |
| C-ter Modification | Amidation |
| N-ter Modification | Free |
| Linear/Cyclic | Cyclic |
| Stereochemistry | L |
| Modified Residues | APC and ACPC |
| FUNCTION | Antibacterial |
| ACTIVITY | >10% hemolysis at 3.1μg/ml |
| RBCs SOURCE | Human |
| Secondary information |
|---|
| Properties | Physico-Chemical details |
| STRUCTURE | |
| DSSP states | NA |
| SMILES | NA |
| External Links |
|---|
| PDB exact | PDB partial | SP exact | SP partial | TrEMBL exact | TrEMBL partial | IEDB exact | IEDB partial |
| NA |
NA |
NA |
NA |
NA |
NA |
NA |
NA |
|
| Reference Informaiton |
|---|
| ARTICLE | Interplay among folding, sequence, and lipophilicity in the antibacterial and hemolytic activities of alpha/beta-peptides. |
| AUTHORS | Schmitt MA,Weisblum B |
| JOURNAL | J Am Chem Soc. 2007 Jan 17;129(2):417-28. |
